title: Factors influencing the binding of calpain I to human erythrocyte inside-out vesicles.
abstract: The mechanism for binding of human erythrocyte calpain I to human erythrocyte inside-out vesicles was studied by immunoelectrophoretic blot analysis. Binding of calpain I to inside-out vesicles was observed both in the absence and presence of Ca2+. Moreover, in the absence of Ca2+, acidic proteins like casein, ovalbumin and calpastatin suppressed while basic proteins like arginase and lysozyme did not affect the binding of calpain I to inside-out vesicles. Here, we propose a model for the binding of calpain to the membrane.
authors.affiliation: Department of Clinical Science, Kyoto University, Japan.
authors.forename: W J
authors.initials: WJ
authors.lastname: Lee
authors.forename: Y
authors.initials: Y
authors.lastname: Adachi
authors.forename: M
authors.initials: M
authors.lastname: Maki
authors.forename: M
authors.initials: M
authors.lastname: Hatanaka
authors.forename: T
authors.initials: T
authors.lastname: Murachi
mesh_terms: D001119:Arginase / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000494:pharmacology; D002154:Calpain / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002364:Caseins / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D007122:Immunoelectrophoresis; D007136:Immunoglobulins / Q000494:pharmacology; D007976:Leupeptins / Q000494:pharmacology; D008954:Models, Biological; D009113:Muramidase / Q000494:pharmacology; D010047:Ovalbumin / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology
chemical_list: D002135:Calcium-Binding Proteins; D002364:Caseins; D007136:Immunoglobulins; D007976:Leupeptins; D011480:Protease Inhibitors; C033668:calpastatin; D010047:Ovalbumin; D009113:Muramidase; D002154:Calpain; D001119:Arginase; C032854:leupeptin; D002118:Calcium